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Database: UniProt
Entry: L0WHL4_9GAMM
LinkDB: L0WHL4_9GAMM
Original site: L0WHL4_9GAMM 
ID   L0WHL4_9GAMM            Unreviewed;       420 AA.
AC   L0WHL4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Mg2+ and Co2+ transporter CorB {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A11A3_02172 {ECO:0000313|EMBL:EKF75637.1};
OS   Alcanivorax hongdengensis A-11-3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF75637.1, ECO:0000313|Proteomes:UP000010164};
RN   [1] {ECO:0000313|EMBL:EKF75637.1, ECO:0000313|Proteomes:UP000010164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-11-3 {ECO:0000313|EMBL:EKF75637.1,
RC   ECO:0000313|Proteomes:UP000010164};
RX   PubMed=23209226; DOI=10.1128/JB.01849-12;
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax
RT   hongdengensis Type Strain A-11-3.";
RL   J. Bacteriol. 194:6972-6972(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKF75637.1}.
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DR   EMBL; AMRJ01000002; EKF75637.1; -; Genomic_DNA.
DR   RefSeq; WP_008927621.1; NZ_AMRJ01000002.1.
DR   AlphaFoldDB; L0WHL4; -.
DR   STRING; 1177179.A11A3_02172; -.
DR   PATRIC; fig|1177179.3.peg.428; -.
DR   eggNOG; COG4536; Bacteria.
DR   OrthoDB; 9797674at2; -.
DR   Proteomes; UP000010164; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR002550; CNNM.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR044751; Ion_transp-like_CBS.
DR   InterPro; IPR005170; Transptr-assoc_dom.
DR   PANTHER; PTHR22777; HEMOLYSIN-RELATED; 1.
DR   PANTHER; PTHR22777:SF17; UPF0053 INNER MEMBRANE PROTEIN YFJD; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF01595; CNNM; 1.
DR   Pfam; PF03471; CorC_HlyC; 1.
DR   SMART; SM01091; CorC_HlyC; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS51846; CNNM; 1.
PE   4: Predicted;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU01193}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU01193};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW   ProRule:PRU01193}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        124..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..191
FT                   /note="CNNM transmembrane"
FT                   /evidence="ECO:0000259|PROSITE:PS51846"
FT   DOMAIN          208..270
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          272..332
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   420 AA;  46781 MW;  9C50AD16A58EF277 CRC64;
     MDTFSDGWLI GALIFLILGS AFFSSSETGM VAINRYRLRH LARQGHRAAS RVEALLKRTD
     RLLSVILIGN NFVNNFAATL AAILAIRWLG DSGAAIAPVV ITIVMLVFAE ITPKTYAAMK
     PERVAFPASL VLKPLQTLLA PLVWLVNGVS SLLLRLGGIR PGEQDDDHLS PEELRTVVNE
     AGGLIPERHQ KMLLNILDLE SVTVEDIMIP RNEMVGIDID DDMADIVATL RSSQHTRLPV
     YNGDPNNMIG LLHLRKLSRL MLRDDINKAE LMQYTVEPYF VPEGTPLNRQ LINFQNAKRR
     IGIVVDEYGD VLGLVTLEDI LEEIVGEFTT DLAATSQDIH PQEDGSYVID GSTHLREINR
     TLHWELPTDG PKTLNGLILE YLQDIPDANI SVKIDQYLIE ILQVKDNMVK AARMRKAEVS
//
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